Mass spectrometry is a valuable tool in structural and functional viral pro
teomics, where it has been used to identify viral capsid proteins, viral mu
tants, and posttranslational modifications. Further, mass-based approaches
combined with time-resolved proteolysis (mass mapping) have revealed the dy
namic nature of viral particles in solution; this method is contributing to
an understanding of the dynamic domains of the viral capsid which may have
significant value in developing new approaches for viral inactivation. As
a result of these experiments, and by comparison with complementary data fr
om X-ray crystallography, a new dimension to viral protein structure and fu
nction is emerging.